amyloid-beta-peptides and leupeptin

amyloid-beta-peptides has been researched along with leupeptin* in 1 studies

Other Studies

1 other study(ies) available for amyloid-beta-peptides and leupeptin

Article	Year
Carboxy-terminal truncation of long-tailed amyloid beta-peptide is inhibited by serine protease inhibitor and peptide aldehyde. FEBS letters, 1998, Mar-13, Volume: 424, Issue:3 The 42/43-residue amyloid beta-peptide (Abeta) is widely believed to play a major role in Alzheimer's disease. The present study shows that the rat brain contains a carboxypeptidase that efficiently deletes three amino acids from Abeta1-43. The carboxypeptidase activity in the brain was completely inhibited by 1 mM phenylmethylsulfonyl fluoride, suggesting the protease is a serine carboxypeptidase. The carboxy-terminal truncation of Abeta1-43 was moderately inhibited by carbobenzoxy-Leu-leucinal, carbobenzoxy-Leu-Leu-leucinal, and carbobenzoxy-Leu-Leu-norvalinal, and weakly by antipain. The present data suggest that the serine carboxypeptidase contributes to the generation of short-tailed Abeta peptides and is important in the intracellular clearance of Abeta1-42/43 in brains. Topics: Amino Acids; Amyloid beta-Peptides; Animals; Antipain; Brain; Carboxypeptidases; Chloromercuribenzoates; Edetic Acid; Leupeptins; p-Chloromercuribenzoic Acid; Pepstatins; Peptide Fragments; Phenylmethylsulfonyl Fluoride; Rats; Serine Proteinase Inhibitors	1998

Article

Year

Carboxy-terminal truncation of long-tailed amyloid beta-peptide is inhibited by serine protease inhibitor and peptide aldehyde.

FEBS letters, 1998, Mar-13, Volume: 424, Issue:3

The 42/43-residue amyloid beta-peptide (Abeta) is widely believed to play a major role in Alzheimer's disease. The present study shows that the rat brain contains a carboxypeptidase that efficiently deletes three amino acids from Abeta1-43. The carboxypeptidase activity in the brain was completely inhibited by 1 mM phenylmethylsulfonyl fluoride, suggesting the protease is a serine carboxypeptidase. The carboxy-terminal truncation of Abeta1-43 was moderately inhibited by carbobenzoxy-Leu-leucinal, carbobenzoxy-Leu-Leu-leucinal, and carbobenzoxy-Leu-Leu-norvalinal, and weakly by antipain. The present data suggest that the serine carboxypeptidase contributes to the generation of short-tailed Abeta peptides and is important in the intracellular clearance of Abeta1-42/43 in brains.

Topics: Amino Acids; Amyloid beta-Peptides; Animals; Antipain; Brain; Carboxypeptidases; Chloromercuribenzoates; Edetic Acid; Leupeptins; p-Chloromercuribenzoic Acid; Pepstatins; Peptide Fragments; Phenylmethylsulfonyl Fluoride; Rats; Serine Proteinase Inhibitors

1998